Glyceraldehyde-3-Phosphate Dehydrogenase Proteins (GAPDH)

The product of GAPDH catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). Additionally we are shipping GAPDH Antibodies (808) and GAPDH Kits (43) and many more products for this protein.

In 60 % of patients with type 2 diabetes, a reversible inhibition of GAPDH is observed.

The results of this study led us to conclude that in cancer cells constantly exposed to conditions of oxidative stress, the protective power of Hsp70 (show HSP70 Proteins) should be abolished by specific inhibitors of Hsp70 (show HSP70 Proteins) expression.

GAPDH and protoporphyrinogen oxidase (show PPOX Proteins) were shown to have higher expression in faster growing cell lines and primary tumors. Pharmacologic inhibition of GAPDH or PPOX reduced the growth of colon cancer cells in vitro

The levels of GAPDH protein were significantly up-regulated in lung squamous cell carcinoma tissues and elevated GAPDH expression is associated with the proliferation and invasion of lung and esophageal squamous cell carcinomas.

Data revealed that GAPDH is a phosphorylation substrate for AMPK (show PRKAA1 Proteins) and its interaction with Sirt1 (show SIRT1 Proteins) in the nucleus. The phosphorylation and the nuclear translocation of GAPDH mediate rapid Sirt1 (show SIRT1 Proteins) activation and autophagy initiation under glucose deprivation.

findings demonstrate that dissociation of the GAPDH/Siah1 pro-apoptotic complex can block high glucose-induced pericyte apoptosis, widely considered a hallmark feature of diabetic retinopathy

The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups; disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA

The strength, selectivity, reversibility, and redox sensitivity of heme binding to GAPDH are consistent with it performing heme sensing or heme chaperone-like functions in cells.

Purified UCH-L1 (show UCHL1 Proteins) and GAPDH were nitrated in vitro with peroxynitrite and the presence of nitrated proteins was confirmed by anti-3-nitrotyrosine Western blots.Subsequent validation with synthetic peptides was conducted for selected nitropeptides.

dissociation of alpha-crystallin and GAPDH

results strongly suggest that Tyr311 and Tyr317 nitration prohibits NAD(+) binding, leading to the loss of catalytic activity of GAPDH.

In the presence of alpha-crystallin or GroEL (show GroEL Proteins) the kinetic of GAPDH aggregation is changed from the diffusion-limited cluster-cluster aggregation to the reaction-limited cluster-cluster aggregation.

The interactions described herein between the beta subunit (show POLG Proteins) of PhK (show PHKA2 Proteins) and GAPDH provide a possible mechanism for the direct linkage of glycogenolysis and glycolysis in skeletal muscle.

astrocytic production of D-serine is modulated by glycolytic activity via interactions between GAPDH and SRR (show SRR Proteins).

Selective inhibition of the glycolytic pathway through GAPDH in chronic lymphocytic leukemia cells with nanoliposomal C6-ceramide could be an effective therapy for leukemia by targeting the Warburg effect.

analysis of a GAPDH/PKCdelta (show PKCd Proteins) signaling switch, which is activated during oxidative stress to regulate the balance between cell survival by mitophagy and cell death due to accumulation of damaged mitochondria

For gene expression analysis in the developing murine neocortex, Gapdh is recommended as a reference gene based on the authors' ranking.

amino acid sequences were used to establish the 3D structures of the active site of glyceraldehyde-3-phosphate dehydrogenase and the phylogenetic relationships of the sardine and octopus enzymes

The expression level of GAPDH was upregulated to a greater extent than those for myogenin (show MYOG Proteins) and myostatin 1 under restricted feeding.

GAPDH Protein Profile

Protein Summary

The product of this gene catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains. Many pseudogenes similar to this locus are present in the human genome. Two transcript variants encoding different isoforms have been found for this gene.